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Integrated Structural Biology Grenoble

Contact person(s) related to this article / Caroline Mas

Presentation MALLS

Presentation

MALS measurements work by calculating the amount of scattered light at each angle detected. The intensity of light scattering of a solution is directly proportional to the average molecular weight and to the concentration of its components.
Our Multi-Angle Laser Light Scattering (MALLS), UV Absorbance and Refractive Index (RI) coupled to a size-exclusion chromatography system allows the simultaneous determination of the molecular weight of each component of a sample.

http://www.wyatt.eu/index.php?id=why-use-mals
 SEC–MALS separation of BSA and haemoglobin (Wyatt)
SEC–MALS separation of BSA and haemoglobin (Wyatt)

Application

  • Determination of concentration and molecular weight
  • Determination of aggregation and oligomerisation states, homogeneity of the sample
  • Determination of conformational changes:
    • Protein-protein interactions
    • Protein-nucelotides interactions
  • It is a method often appropriated for studying interactions of membrane protein and/or glycosylated proteins

Key words

Size-exclusion chromatography, Multi-Angle Laser Light Scattering, Protein concentration, Oligomerisation states, stoichiometry of complexes

Staff

Platform engineer: Caroline Mas
Professor Marc Jamin
Office: CIBB room 020
Platform: CIBB room 001

Specific Equipment

Wyatt Dawn Heleos II - Multi-Angle static Light Scattering
Wyatt Optilab T-rex – Refractometer
Hitachi Elite LaChrom UV detector L-2400
Hitachi Elite LaChrom Pump L-2130

Access mode

Please read the general conditions of use:

  • The platform is accessible to local PSB users as well as national and international (Instruct) users.
  • Service: routine experiments performed for punctual users
  • Instrument allocation after user training: for users who have completed training to gain operational autonomy time is allocated to them to perform and analyze their experiments
  • Scientific collaboration: projects in which the Biophysical platform is strongly involved. In this case, experiments are designed, performed and analyzed in tandem between the scientific responsible and the applicant.
  • You have to bring your own Size exclusion chromatography column

Location

The Biophysical platform is located in the Carl-Ivar Brändén Building, ground floor, room 001 (Shared Building C).

How to make a request

To make a booking request, submit the sample form and fill the request form.

Sample form:

SEC-MALLS booking

Samples

Only non-pathogenic biological samples are accepted. Decree of the July 18, 1994 establishing the list of biological pathogens, amended by Decrees of April 17, 1997 and June 30, 1998 (Decrees in French). The list of biological pathogens is available on the website of the IPBS.

For one injection:

  • the sample is typically at 2-10 mg/mL
  • the volume required is 55 µl
  • the purity should be 90%
  • the elution buffer should be degased and filtered at 0.22µm (1L is required)
  • 50 min per run (0.5mL/min)
    The samples must be centrifuge or filtered at 0.1µm.
    Samples are not stored –unless specific request.

Note that it is mandatory to send a chromatogram or SDS-PAGE photo of all the samples to be analysed before the day of the experiment.

Cost

Academics: Participation to the maintenance fees
Industrials: Please contact us for cost information

Follow up / acknowledgements

The user agrees to promote the obtained results by mentioning the platform in the acknowledgements in case of publication or scientific communication and to communicate the reference of the article to the responsible for the platform.

Service / Providing access mode: Acknowledgements in publications and oral presentations

Collaboration: Co-authors in publications and oral presentations.

Acknowledgements in publications:

Please find below the sentence that has to be written in all publications based on our UMS platforms:
"This work used the platforms of the Grenoble Instruct-ERIC Center (ISBG : UMS 3518 CNRS-CEA-UGA-EMBL) with support from FRISBI (ANR-10-INBS-05-02) and GRAL (ANR-10-LABX-49-01) within the Grenoble Partnership for Structural Biology (PSB). We thank Caroline Mas and/or Marc Jamin, for assistance and/or access to the Biophysical platform."